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434 related items for PubMed ID: 15283922

  • 1. High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins.
    Kamatari YO, Kitahara R, Yamada H, Yokoyama S, Akasaka K.
    Methods; 2004 Sep; 34(1):133-43. PubMed ID: 15283922
    [Abstract] [Full Text] [Related]

  • 2. Highly fluctuating protein structures revealed by variable-pressure nuclear magnetic resonance.
    Akasaka K.
    Biochemistry; 2003 Sep 23; 42(37):10875-85. PubMed ID: 12974621
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  • 3. Monitoring protein folding at atomic resolution.
    Kumar TK, Yu C.
    Acc Chem Res; 2004 Dec 23; 37(12):929-36. PubMed ID: 15609984
    [Abstract] [Full Text] [Related]

  • 4. Noncooperative Formation of the off-pathway molten globule during folding of the alpha-beta parallel protein apoflavodoxin.
    Nabuurs SM, Westphal AH, van Mierlo CP.
    J Am Chem Soc; 2009 Feb 25; 131(7):2739-46. PubMed ID: 19170491
    [Abstract] [Full Text] [Related]

  • 5. High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded.
    Kitahara R, Yamada H, Akasaka K, Wright PE.
    J Mol Biol; 2002 Jul 05; 320(2):311-9. PubMed ID: 12079388
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  • 7. Using nuclear magnetic resonance spectroscopy to study molten globule states of proteins.
    Redfield C.
    Methods; 2004 Sep 05; 34(1):121-32. PubMed ID: 15283921
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  • 8. Probing invisible, low-populated States of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein folding.
    Korzhnev DM, Kay LE.
    Acc Chem Res; 2008 Mar 05; 41(3):442-51. PubMed ID: 18275162
    [Abstract] [Full Text] [Related]

  • 9. High pressure NMR reveals a variety of fluctuating conformers in beta-lactoglobulin.
    Kuwata K, Li H, Yamada H, Batt CA, Goto Y, Akasaka K.
    J Mol Biol; 2001 Feb 02; 305(5):1073-83. PubMed ID: 11162115
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  • 11. Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings.
    Mohana-Borges R, Goto NK, Kroon GJ, Dyson HJ, Wright PE.
    J Mol Biol; 2004 Jul 23; 340(5):1131-42. PubMed ID: 15236972
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  • 12. Identification of native and non-native structure in kinetic folding intermediates of apomyoglobin.
    Nishimura C, Dyson HJ, Wright PE.
    J Mol Biol; 2006 Jan 06; 355(1):139-56. PubMed ID: 16300787
    [Abstract] [Full Text] [Related]

  • 13. Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy.
    Schanda P, Forge V, Brutscher B.
    Proc Natl Acad Sci U S A; 2007 Jul 03; 104(27):11257-62. PubMed ID: 17592113
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  • 14. NMR studies of partially folded molten-globule states.
    Redfield C.
    Methods Mol Biol; 2004 Jul 03; 278():233-54. PubMed ID: 15317999
    [Abstract] [Full Text] [Related]

  • 15. Characterization of the folding and unfolding reactions of single-chain monellin: evidence for multiple intermediates and competing pathways.
    Patra AK, Udgaonkar JB.
    Biochemistry; 2007 Oct 23; 46(42):11727-43. PubMed ID: 17902706
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  • 20. [How many molten globules states exist?].
    Uverskiĭ VN.
    Biofizika; 1998 Oct 23; 43(3):416-21. PubMed ID: 9702331
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